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Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action
Open accessAbstract
Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly because the substrate specificity of Hsp90 is poorly understood. Here, we obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. Complementarily, a 106-Å-long substrate-binding interface in Hsp90 enables many low-affinity contacts. This allows recognition of scattered hydrophobic residues in late folding intermediates that remain after early burial of the Hsp70 sites. Our model resolves the paradox of how Hsp90 specifically selects for late folding intermediates but also for some intrinsically disordered proteins-through the eyes of Hsp90 they look the same.
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“By NMR, Hsp90 is identified to interact with tau transiently in the apo state and function as a scaffold in complex with FKBP51”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Karagoz et al., 2014
Experimental — accuracy not yet measuredIn the citing paper
“In the absence of nucleotides, all clients show similar affinities in the low micromolar range for Hsp90 (Table 1), consistent with previous studies (16, 20, 48).”
From Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network (2021) · cites this paper as [48]
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“8 – 10).”
InfluentialLorenzo, D. D., Bisi, N., Bucci, R., Ennen, I., Presti, L. L., Dodero, V. I., Brandt, R., Ongeri, S., Gelmi, M. L., & Tonali, N. (2025) · iScience · doi:10.1016/j.isci.2025.112272 · Cited by 1
“35 To verify the ability of the (R) -configured Isox-b 2 -AA to induce a stable b -turn like folding in a long peptide sequence and, thus, to be employable as b -turn inducer for potential inhibitors of amyloid aggregation, the S4 and S7 peptide sequences of N-terminal portion of Hsp90 were attached to the (R) -configur…”
InfluentialTargeting Hsp-90 Related Disease Entities for Therapeutic Development
Westlake, T. J., Sun, M., Rosenblum, B. C., Zhuang, Z., & Rosenblum, J. S. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_10 · Cited by 1
Quarterly intrinsic disorder digest (January-February-March, 2014)
DeForte, S., Reddy, K. D., & Uversky, V. N. (2016) · Intrinsically Disordered Proteins · doi:10.1080/21690707.2016.1153395 · Cited by 1
“of Hsp90 with tau, and found that the interaction interface is broad and contains a number of low affinity contacts, including dispersed hydrophobic residues characteristic of late folding intermediates.(90) This study provides a mechanism of action as to how Hsp90 can select for IDPs as well as late folding intermedi…”
BackgroundBrijmohan, A. S. (2017) · TSpace (University of Toronto) · Cited by 1
Refolding activity of bacterial Hsp90 in vivo reveals ancient chaperoning functionPreprint
Luengo, T. M., Ahlnäs, T., Hoekstra, A. T., Berkers, C. R., Mayer, M. P., & Rüdiger, S. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/462549 · Cited by 1
“Hsp90 offers a larger surface with many contacts distributed over the molecule that allow proteins to reach the native state [43, 44].”
BackgroundSelf-citationLyu, C., Vela, S. D., Al‐Hilaly, Y. K., Marshall, K. E., Thorogate, R., Svergun, D. I., Serpell, L. C., Pastore, A., & Hanger, D. P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.08.451675 · Cited by 1
Hsp multichaperone complex buffers pathologically modified TauPreprint
Moll, A., Ramirez, L. M., Ninov, M., Schwarz, J., Urlaub, H., & Zweckstetter, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.18.484853 · Cited by 1
Self-citationRai, S. K., Khanna, R., Sarbahi, A., Joshi, A., & Mukhopadhyay, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.13.598862 · Cited by 1
“Several such potentially pathogenic events in cells are promptly halted or counteracted by the cellular chaperone machinery comprising several Hsps (43-48, 75 ).”
BackgroundAge-associated increases in FKBP51 facilitate tau neurotoxicity
Blair, L. J. (2014) · Digital Commons - University of South Florida (University of South Florida)
The molecular mechanism of Hsp90-induced oligomerization of TauPreprint
Weickert, S., Wawrzyniuk, M., John, L., Rüdiger, S., & Drescher, M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/614289
“Both residues are located in Tau-RD, which has been identified as the Hsp90-binding region before (25).”
BackgroundResultInfluentialSelf-citationStructural Basis for Protein Folding and Holding Mediated by Molecular Chaperones
Saio, T., & Ishimori, K. (2019) · Seibutsu Butsuri · doi:10.2142/biophys.59.197
Engineering Chaperones for Alzheimer’s Disease: Insights from Drosophila Models
Martín‐Peña, A., & Rincón-Limas, D. E. (2019) · Heat shock proteins · doi:10.1007/978-3-030-24285-5_15
The adaptive potential of the middle domain of yeast Hsp90Preprint
Cote-Hammarlof, P. A., Fragata, I., Flynn, J. M., Mavor, D., Zeldovich, K. B., Bank, C., & Bolon, D. N. A. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/832022
The Analysis of Exosomal Tau Release and its Regulation
Bradshaw, A. (2018) · UCL Discovery (University College London)
Mercier, R. J. (2019) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3-tms0-be49
Gregorio, S. E. D., Esmaeili, M., Salem, A., & Duennwald, M. L. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.24.457481
“…or reduced expression of Hsp90 co-chaperones also exacerbates Matrin3 toxicity and reduces inclusion formation, possibly by stabilizing toxic conformations as determined before for the misfolded tau protein (Karagöz et al., 2014, Shelton et al., 2017, Weickert et al., 2020, Tortosa et al., 2009).”
BackgroundExploring the human Hsp70-Hop-Hsp90 system for Tau recognition
Moll, A. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9131
Protein Folding and Chaperones
Sinnige, T., Karagöz, G. E., & Rüdiger, S. (2015) · Wiley eBooks · doi:10.1002/9780470015902.a0005721.pub3
Self-citationFaculty Opinions recommendation of Regulation of α-synuclein by chaperones in mammalian cells.
Jackson, S. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737028220.793569910
Mollapour, M. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737482045.793572272
Multiplex Immunostaining Method to Distinguish HSP Isoforms in Cancer Tissue Specimens
Kawai, H., Ono, K., & Eguchi, T. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3342-7_21
Solution NMR Studies of Chaperone–Client Systems
Wan, C., & Huang, C. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00086
Single Molecule Fluorescence Methods for Molecular Chaperones and Their Client Interactions
Mondol, T., Sohmen, B., & Hugel, T. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00181
Integrative Methods to Investigate Chaperones in Regulating Protein Phase Separation and Aggregation
Li, D., Zhang, S., & Liu, C. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00319
Dröden, J., & Drescher, M. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00217
NMR Study of the Structure and Dynamics of Chaperone–Client Complexes
Saio, T. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00162
Huo, Y., Karnawat, R., Liu, L., Knieß, R. A., Gross, M., Chen, X., & Mayer, M. P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.25.600625
Lorenzo, D. D., Bisi, N., Bucci, R., Ennen, I., Presti, L. L., Dodero, V. I., Brandt, R., Ongeri, S., Gelmi, M. L., & Tonali, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.04.616679
“Surprisingly, at a sub-stoichiometric ratio and in the presence of low concentrated heparin, the same compound inspired by the chaperone protein Hsp90, can maintain a secondary nucleation-dominated kinetic, as observed with the seed-competent mimic, showing, however, morphology of the fibrils similar to the straight f…”
BackgroundInfluentialSubtle Variations in a Client Protein Determine Bacterial Hsp90 Dependence
Corteggiani, M., Ali Chaouche, A., Bahun, M., Honoré, F. A., Byrne, D., Dementin, S., Rebeaud, M. E., & Genest, O. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169378
Metadata
- Authors
- Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., Dickey, C. A., Mandelkow, E., Zweckstetter, M., Boelens, R., Madl, T., & Rüdiger, S. G. D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Utrecht University (NL)
- Max Planck Institute for Biophysical Chemistry (DE)
- German Center for Neurodegenerative Diseases (DE)
- University of South Florida (US)
- Paul Scherrer Institute (CH)
- University of Graz (AT)
- Corresponding author
- Madl, Tobias
- Rüdiger, Stefan G.D.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-02
- Volume
- 156
- Issue
- 5
- Pages
- 963-974
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4263503
- OpenAlex
- W1993050837
- Cited by
- 318
- References
- 68
- Citations by year
- 2026: 13 · 2025: 21 · 2024: 22 · 2023: 31 · 2022: 27 · 2021: 19 · 2020: 27 · 2019: 33 · 2018: 32 · 2017: 31 · 2016: 26 · 2015: 26 · 2014: 10
- FWCI
- 12.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Research Publications (Maastricht University) (submittedVersion, other-oa)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Max Planck Digital Library (submittedVersion, other-oa)
- Max Planck Digital Library (submittedVersion)
- Repository@Nottingham (University of Nottingham) (submittedVersion, cc-by)
- Site cant be reached (submittedVersion)
- DZNE Pub (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- European Commission (261863)
- National Institute of Neurological Disorders and Stroke (R01NS073899, NS073899)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- HSP90, tau protein, molecular chaperones, protein folding, substrate specificity, intrinsically disordered proteins, HSP70, folding intermediates, hydrophobic residues
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, X-Ray Diffraction, tau Proteins, Protein Folding, HSP90 Heat-Shock Proteins, Scattering, Small Angle
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